- Nogo A
Nogo A is a
protein that has been identified as aninhibitor ofneurite outgrowth specific to the centralnervous system . Research suggests that blocking Nogo-A during neuronal damage (from diseases such asMultiple Sclerosis ) will help to protect or restore the damaged neurons (Karnezis et al, 2004).The Nogo gene contains the isoforms Nogo A, B and C. Nogo-A has two known inhibitory domains including amino-Nogo, at the N-terminus and Nogo-66, which makes up the molecules extracellular loop. Both amino-Nogo and Nogo-66 are involved in inhibitory responses, where amino-Nogo is a strong inhibitor of neurite outgrowth, and Nogo-66 is involved in growth cone destruction (Karnezis et al, 2004).
Potential Uses
The investigation into the mechanisms of this protein presents a great potential for the treatment of
auto-immune mediated demyelinating diseases and spinal cord injury regeneration. It has also been found to be a key player in the process whereby physical exercise enhances learning and memory processes in the brain. [ [http://www.eurekalert.org/pub_releases/2008-03/uorm-sar031808.php Stopping a receptor called 'nogo' boosts the synapses ] ]References
*cite journal | author= Karnezis et al |title=The neurite outgrowth inhibitor Nogo A is involved in autoimmune-mediated demyelination. |journal="Nature Neuroscience |volume=7 |issue= 7 |pages= 736–744. |year= 2004 |pmid= 15184901 |doi=10.1038/nn1261
*cite journal | author= Li M, Shi J, Wei Z, Teng FY, Tang BL, Song J. |title=Structural characterization of the human Nogo-A functional domains. Solution structure of Nogo-40, a Nogo-66 receptor antagonist enhancing injured spinal cord regeneration. |journal=Eur J Biochem. |volume=271 |issue= 17 |pages= 3512–22. |year= 2004 |pmid= 15317586 |doi=10.1111/j.0014-2956.2004.04286.x
*cite journal | author= Li M, Liu J, Song J. |title=Nogo goes in the pure water: solution structure of Nogo-60 and design of the structured and buffer-soluble Nogo-54 for enhancing CNS regeneration. |journal=Protein Sci. |volume=15 |issue= 8 |pages= 1835–41. |year= 2006 |pmid= 16877707 |doi=10.1110/ps.062306906
*cite journal | author= Li M, Song J. |title=The N- and C-termini of the human Nogo molecules are intrinsically unstructured: bioinformatics, CD, NMR characterization, and functional implications. |journal=Proteins. |volume=68 |issue= 1 |pages= 100–8. |year= 2007 |pmid= 17397058 |doi=10.1002/prot.21385
*cite journal | author= Li M, Song J. |title=Nogo-B receptor possesses an intrinsically unstructured ectodomain and a partially folded cytoplasmic domain. |journal=Biochem Biophys Res Commun. |volume=360 |issue= 1 |pages= 128–34. |year= 2007 |pmid= 17585875 |doi=10.1016/j.bbrc.2007.06.031
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